Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07177"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"(5E,13E)-11-HYDROXY-9,15-DIOXOPROSTA-5,13-DIEN-1-OIC ACID"
|
| rdf:type | |
| drugbank:description |
"
experimental
This compound belongs to the prostaglandins and related compounds. These are unsaturated carboxylic acids consisting of of a 20 carbon skeleton that also contains a five member ring, and are based upon the fatty acid arachidonic acid.
Prostaglandins and related compounds
Organic Compounds
Lipids
Eicosanoids
Prostaglandins and related compounds
Keto Fatty Acids
Carbocyclic Fatty Acids
Unsaturated Fatty Acids
Enones
Acryloyl Compounds
Cyclic Alcohols and Derivatives
Secondary Alcohols
Carboxylic Acids
Enolates
Polyamines
acryloyl-group
cyclic alcohol
enone
secondary alcohol
ketone
polyamine
carboxylic acid derivative
carboxylic acid
enolate
carbonyl group
alcohol
logP
3.27
ALOGPS
logS
-3.8
ALOGPS
Water Solubility
5.83e-02 g/l
ALOGPS
logP
3.64
ChemAxon
IUPAC Name
(5E)-7-[(1S,2S,3R)-3-hydroxy-5-oxo-2-[(1E)-3-oxooct-1-en-1-yl]cyclopentyl]hept-5-enoic acid
ChemAxon
Traditional IUPAC Name
(5E)-7-[(1S,2S,3R)-3-hydroxy-5-oxo-2-[(1E)-3-oxooct-1-en-1-yl]cyclopentyl]hept-5-enoic acid
ChemAxon
Molecular Weight
350.4492
ChemAxon
Monoisotopic Weight
350.20932407
ChemAxon
SMILES
[H][C@@]1(O)CC(=O)[C@@]([H])(C\C=C\CCCC(O)=O)[C@]1([H])\C=C\C(=O)CCCCC
ChemAxon
Molecular Formula
C20H30O5
ChemAxon
InChI
InChI=1S/C20H30O5/c1-2-3-6-9-15(21)12-13-17-16(18(22)14-19(17)23)10-7-4-5-8-11-20(24)25/h4,7,12-13,16-17,19,23H,2-3,5-6,8-11,14H2,1H3,(H,24,25)/b7-4+,13-12+/t16-,17-,19+/m0/s1
ChemAxon
InChIKey
InChIKey=YRTJDWROBKPZNV-DYTRGIJQSA-N
ChemAxon
Polar Surface Area (PSA)
91.67
ChemAxon
Refractivity
98.54
ChemAxon
Polarizability
39.69
ChemAxon
Rotatable Bond Count
12
ChemAxon
H Bond Acceptor Count
5
ChemAxon
H Bond Donor Count
2
ChemAxon
pKa (strongest acidic)
4.3
ChemAxon
pKa (strongest basic)
-2.9
ChemAxon
Physiological Charge
-1
ChemAxon
Number of Rings
1
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
PubChem Compound
46937058
PubChem Substance
99443648
PDB
5OP
BE0003795
Prostaglandin reductase 1
Human
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Prostaglandin reductase 1
Involved in 15-oxoprostaglandin 13-oxidase activity
Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha (By similarity). Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4
PTGR1
9q31.3
Cytoplasm
None
8.53
35869.6
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:18429
GeneCards
PTGR1
GenBank Gene Database
BC035228
GenBank Protein Database
23271371
UniProtKB
Q14914
UniProt Accession
PTGR1_HUMAN
15-oxoprostaglandin 13-reductase
NADP-dependent leukotriene B4 12-hydroxydehydrogenase
PRG-1
>Prostaglandin reductase 1
MVRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEG
DTMMGQQVAKVVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALG
TVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVA
YLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICG
AISTYNRTGPLPPGPPPEIVIYQELRMEAFVVYRWQGDARQKALKDLLKWVLEGKIQYKE
YIIEGFENMPAAFMGMLKGDNLGKTIVKA
>990 bp
ATGGTTCGTACTAAGACATGGACCCTGAAGAAGCACTTTGTTGGCTATCCTACTAATAGT
GACTTTGAGTTGAAGACATCTGAGCTCCCACCCTTAAAAAATGGAGAGGTCCTGCTTGAA
GCTTTGTTCCTCACCGTGGATCCCTACATGAGAGTGGCAGCCAAAAGATTGAAGGAAGGT
GATACAATGATGGGGCAGCAAGTGGCCAAAGTTGTGGAAAGTAAAAATGTAGCCCTACCA
AAAGGAACTATTGTACTGGCTTCTCCAGGCTGGACAACGCACTCCATTTCTGATGGGAAA
GATCTGGAAAAGCTGCTGACAGAGTGGCCAGACACAATACCACTGTCTTTGGCTCTGGGG
ACAGTTGGCATGCCAGGCCTGACTGCCTACTTTGGCCTACTTGAAATCTGTGGTGTGAAG
GGTGGAGAAACAGTGATGGTTAATGCAGCAGCTGGAGCTGTGGGCTCAGTCGTGGGGCAG
ATTGCAAAGCTCAAGGGCTGCAAAGTTGTTGGAGCAGTAGGGTCTGATGAAAAGGTTGCC
TACCTTCAAAAGCTTGGATTTGATGTCGTCTTTAACTACAAGACGGTAGAGTCTTTGGAA
GAAACCTTGAAGAAAGCGTCTCCTGATGGTTATGATTGTTATTTTGATAATGTAGGTGGA
GAGTTTTCAAACACTGTTATCGGCCAGATGAAGAAATTTGGAAGGATTGCCATATGTGGA
GCCATCTCTACATATAACAGAACCGGCCCACTTCCCCCAGGCCCACCCCCAGAGATTGTT
ATCTATCAGGAGCTTCGCATGGAAGCTTTTGTCGTCTACCGCTGGCAAGGAGATGCCCGC
CAAAAAGCTCTGAAGGACTTGCTGAAATGGGTCTTAGAGGGTAAAATCCAGTACAAGGAA
TATATCATTGAAGGATTTGAAAACATGCCAGCCGCATTTATGGGAATGCTGAAAGGAGAT
AATTTGGGGAAGACAATAGTGAAAGCATGA
PF00107
ADH_zinc_N
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
zinc ion binding
function
binding
function
catalytic activity
BE0003560
Prostaglandin reductase 2
Human
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Prostaglandin reductase 2
Involved in 15-oxoprostaglandin 13-oxidase activity
Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto- PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation (By similarity)
PTGR2
14q24.3
Cytoplasm (By similarity)
None
5.08
38498.7
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:20149
GeneCards
PTGR2
GenBank Gene Database
AY346133
GenBank Protein Database
37912002
UniProtKB
Q8N8N7
UniProt Accession
PTGR2_HUMAN
15-oxoprostaglandin 13-reductase
PRG-2
Zinc-binding alcohol dehydrogenase domain-containing protein 1
>Prostaglandin reductase 2
MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDT
GTDYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKVDPQ
LVDGHLSYFLGAIGMPGLTSLIGIQEKGHITAGSNKTMVVSGAAGACGSVAGQIGHFLGC
SRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTV
ISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGI
LQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIVCISEEISL
>1056 bp
ATGATTGTTCAAAGAGTGGTATTGAATTCTCGACCTGGAAAAAATGGTAATCCAGTGGCA
GAGAATTTCCGAATGGAAGAAGTCTATTTACCAGATAATATTAATGAAGGACAAGTACAA
GTTAGAACTCTTTATCTTTCTGTGGATCCTTACATGCGTTGTAGAATGAATGAAGACACT
GGCACTGATTATATAACACCTTGGCAGCTATCTCAAGTCGTTGATGGTGGAGGTATTGGA
ATTATAGAAGAAAGCAAACACACAAATTTGACTAAAGGCGATTTTGTGACTTCTTTCTAT
TGGCCCTGGCAAACCAAGGTTATTCTGGATGGAAATAGCCTTGAAAAGGTAGACCCACAA
CTTGTGGATGGACACCTTTCATATTTTCTTGGAGCTATAGGTATGCCTGGTTTGACTTCC
TTGATTGGGATACAGGAAAAAGGTCATATAACTGCTGGATCTAATAAGACAATGGTTGTC
AGTGGGGCCGCAGGTGCCTGTGGATCTGTGGCTGGGCAGATTGGCCATTTCTTAGGTTGT
TCCAGAGTGGTGGGGATTTGTGGAACACATGAGAAATGCATCCTCTTGACCTCAGAACTG
GGCTTTGATGCTGCAATTAATTATAAAAAAGACAATGTGGCAGAACAGCTCCGTGAATCA
TGCCCAGCTGGAGTGGATGTTTATTTTGACAATGTTGGTGGTAACATCAGTGATACAGTG
ATAAGTCAGATGAATGAGAACAGCCACATCATCCTGTGTGGTCAAATTTCTCAGTACAAC
AAAGATGTGCCTTATCCTCCCCCGCTATCCCCTGCTATAGAGGCAATCCAGAAAGAAAGA
AACATCACAAGGGAAAGATTTCTGGTATTAAATTATAAAGACAAATTTGAGCCTGGCATT
CTACAGCTGAGTCAGTGGTTTAAAGAAGGAAAGCTAAAGATTAAAGAGACGGTAATAAAT
GGGTTGGAAAACATGGGAGCTGCATTCCAGTCCATGATGACAGGAGGTAACATTGGAAAG
CAGATAGTTTGCATTTCAGAAGAAATCTCTTTGTAA
PF00107
ADH_zinc_N
function
binding
function
catalytic activity
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
zinc ion binding
"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt
The resource does not appear as an object